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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 2
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pubmed:dateCreated |
2011-2-8
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pubmed:databankReference |
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pubmed:abstractText |
Streptococcus mutans is one of the pathogenic species involved in dental caries, especially in the initiation and development stages. Here, the crystal structure of SMU.595, a putative dihydroorotate dehydrogenase (DHOD) from S. mutans, is reported at 2.4?Å resolution. DHOD is a flavin mononucleotide-containing enzyme which catalyzes the oxidation of L-dihydroorotate to orotate, which is the fourth step and the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. The reductive lysine-methylation procedure was applied in order to improve the diffraction qualities of the crystals. Analysis of the S. mutans DHOD crystal structure shows that this enzyme is a class 1A DHOD and also suggests potential sites that could be exploited for the design of highly specific inhibitors using the structure-based chemotherapeutic design technique.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
182-7
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pubmed:meshHeading |
pubmed-meshheading:21301083-Amino Acid Sequence,
pubmed-meshheading:21301083-Binding Sites,
pubmed-meshheading:21301083-Catalysis,
pubmed-meshheading:21301083-Conserved Sequence,
pubmed-meshheading:21301083-Crystallography, X-Ray,
pubmed-meshheading:21301083-Dental Caries,
pubmed-meshheading:21301083-Dimerization,
pubmed-meshheading:21301083-Escherichia coli,
pubmed-meshheading:21301083-Flavin Mononucleotide,
pubmed-meshheading:21301083-Histidine,
pubmed-meshheading:21301083-Humans,
pubmed-meshheading:21301083-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:21301083-Lysine,
pubmed-meshheading:21301083-Methylation,
pubmed-meshheading:21301083-Models, Molecular,
pubmed-meshheading:21301083-Molecular Sequence Data,
pubmed-meshheading:21301083-Orotic Acid,
pubmed-meshheading:21301083-Oxidation-Reduction,
pubmed-meshheading:21301083-Oxidoreductases Acting on CH-CH Group Donors,
pubmed-meshheading:21301083-Protein Conformation,
pubmed-meshheading:21301083-Protein Folding,
pubmed-meshheading:21301083-Protein Structure, Quaternary,
pubmed-meshheading:21301083-Protein Structure, Secondary,
pubmed-meshheading:21301083-Protein Subunits,
pubmed-meshheading:21301083-Pyrimidines,
pubmed-meshheading:21301083-Recombinant Proteins,
pubmed-meshheading:21301083-Sequence Homology, Amino Acid,
pubmed-meshheading:21301083-Streptococcus mutans,
pubmed-meshheading:21301083-Substrate Specificity,
pubmed-meshheading:21301083-X-Ray Diffraction
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pubmed:year |
2011
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pubmed:articleTitle |
Structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans.
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pubmed:affiliation |
Department of Genetics, School of Life Science, Fudan University, Shanghai, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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